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Despite sharing 44% amino acid identity with GLI3, only a small fraction of GLI2 appears to be processed to a repressor form in the absence of Hh signaling; the bulk of the protein is completely degraded in a phosphorylation- and proteasome-dependent manner (Pan et al, 2007; Pan et al, 2009; Pan and Wang, 2007). Degradation of GLI2 depends on phosphorylation of four consensus PKA sites in the C-terminal region. This phosphorylation primes GLI2 for subsequent phosphorylation by CK1 and GSK3, creating a binding site for betaTrCP and promoting its subsequent ubiquitination and degradation (Pan et al, 2006; Pan and Wang, 2007; Pan et al, 2009).